ID Q7NH47_GLOVI Unreviewed; 940 AA.
AC Q7NH47;
DT 15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2003, sequence version 1.
DT 27-MAR-2024, entry version 111.
DE SubName: Full=Glr2690 protein {ECO:0000313|EMBL:BAC90631.1};
GN OrderedLocusNames=glr2690 {ECO:0000313|EMBL:BAC90631.1};
OS Gloeobacter violaceus (strain ATCC 29082 / PCC 7421).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Gloeobacterales; Gloeobacteraceae;
OC Gloeobacter.
OX NCBI_TaxID=251221 {ECO:0000313|EMBL:BAC90631.1, ECO:0000313|Proteomes:UP000000557};
RN [1] {ECO:0000313|EMBL:BAC90631.1, ECO:0000313|Proteomes:UP000000557}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29082 / PCC 7421 {ECO:0000313|Proteomes:UP000000557};
RX PubMed=14621292; DOI=10.1093/dnares/10.4.137;
RA Nakamura Y., Kaneko T., Sato S., Mimuro M., Miyashita H., Tsuchiya T.,
RA Sasamoto S., Watanabe A., Kawashima K., Kishida Y., Kiyokawa C., Kohara M.,
RA Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Takeuchi C., Yamada M.,
RA Tabata S.;
RT "Complete genome structure of Gloeobacter violaceus PCC 7421, a
RT cyanobacterium that lacks thylakoids.";
RL DNA Res. 10:137-145(2003).
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DR EMBL; BA000045; BAC90631.1; -; Genomic_DNA.
DR RefSeq; NP_925636.1; NC_005125.1.
DR RefSeq; WP_011142684.1; NC_005125.1.
DR AlphaFoldDB; Q7NH47; -.
DR STRING; 251221.gene:10760192; -.
DR EnsemblBacteria; BAC90631; BAC90631; BAC90631.
DR KEGG; gvi:glr2690; -.
DR PATRIC; fig|251221.4.peg.2719; -.
DR eggNOG; COG0344; Bacteria.
DR eggNOG; COG0574; Bacteria.
DR eggNOG; COG3848; Bacteria.
DR HOGENOM; CLU_005950_0_0_3; -.
DR InParanoid; Q7NH47; -.
DR OrthoDB; 9765468at2; -.
DR PhylomeDB; Q7NH47; -.
DR Proteomes; UP000000557; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0043772; F:acyl-phosphate glycerol-3-phosphate acyltransferase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016301; F:kinase activity; IEA:InterPro.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:InterPro.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 2.
DR Gene3D; 3.50.30.10; Phosphohistidine domain; 1.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR003811; G3P_acylTferase_PlsY.
DR InterPro; IPR008279; PEP-util_enz_mobile_dom.
DR InterPro; IPR036637; Phosphohistidine_dom_sf.
DR InterPro; IPR002192; PPDK_AMP/ATP-bd.
DR PANTHER; PTHR43615; PHOSPHOENOLPYRUVATE SYNTHASE-RELATED; 1.
DR PANTHER; PTHR43615:SF1; PHOSPHOENOLPYRUVATE SYNTHASE-RELATED; 1.
DR Pfam; PF02660; G3P_acyltransf; 1.
DR Pfam; PF00391; PEP-utilizers; 1.
DR Pfam; PF01326; PPDK_N; 1.
DR SMART; SM01207; G3P_acyltransf; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52009; Phosphohistidine domain; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000000557};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..24
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 81..100
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 106..130
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 246..373
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 852..923
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
SQ SEQUENCE 940 AA; 100944 MW; F1D7FFE594EB93CB CRC64;
MLPSVLVLIA AFVLGGVPLS GWLFRLATGK DLRNLGTGNV SVAAAFLHGG RVVGIGAALV
EASRGIAAVF AAQTFSSAPE WPLLALSALV AGRFWIGRAA GATNAWWGLV VFAPVVTYLV
TLVGLVPWAI YRGRTGRRRA ELATLVALPV AFYFQSGQLL TTGAAALLSL WLGYALLRVP
DDMELTRQSS KPPSLDLDLD PGAVGPKAAN LSKLKKAGLP VPGGWVLLSE NTPEQLLAIA
APSPEAPWIV RSSATGEDTV ANSAAGQYLS VADVTNPAGF IEATARVRAS YDIPAATAYR
RDRKIADGRM AVLVQPQIRG VWSGVVFTRD PVDGSEVLVV EALPGGAAAV VGGQRTPERA
VIDRASGAVE SSAIPHPILA ALQGAALKVE GLFEGVPQDI EWTWDGERLW LLQARPVTAL
QPVWTRTIAA EVIPGTIRPL TWSINRPLTC GVWGEIFTIV LGKRAVGIDF GETATLLDGW
AYFNATLLGD IFLRMGLPPE SLDFLYRGSR FSRPPPGSVL ANLPGLLRLL GRDLSLEGDF
RRTDKDLLGP LMATLADENV DRLTPKQLVG RAERIQVGLR LVTYFNILAP LGLSLRRALL
GVNEDWLGTE ATAEVRAVRE LGAMATEARS RLGNLADTGD LPQVKAALQT TPIPAQLDRF
IERFGYLSEV GTDIAVPTWS EHPETIRDLF LAMVQIPRQP VERSQPRRPW DSLRSALCRP
RARTRARVSE IYDQLLAYLR WTFTALERQW RSGGLLESEG DIFFLTQDEI LALARGELAG
EPRALVASRR AEYERQCRRR VPRVVYGMQI PEQTAEPETI AATGRLKGIA ASRGRVEGVV
RVLKSVSATV RLDADTVLVV PYTDAGWAPV LAQARAIVCE AGGRLSHGAI VAREYGLPAV
MNVIGATALL ADGQRVRVDG GAGTVEILGA DPHAGEKPTA
//
